Evidence map›Paper›PMID 39678489›Full record

ReviewMedComm2024

Deubiquitinases as novel therapeutic targets for diseases.

Yali Xian, Jing Ye, Yu Tang, Nan Zhang, Cheng Peng, Wei Huang, Gu He

Abstract readReview
In one paragraph

Review in MedComm, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

29 citing papers in PubMed.

  1. Article
  2. Nit2/ω-amidase as a potential non-invasive diagnostic marker for moyamoya disease.Child's nervous system : ChNS : official journal of the International Society for Pediatric Neurosurgery · 2026
    Article
  3. Deubiquitinases as Regulators and Therapeutic Targets in Vascular Diseases.International journal of molecular sciences · 2026
    Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Review
  10. [Ubiquitination-mediated regulation of T cell homeostasis and autoimmune diseases].Zhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences · 2026
    Review
  11. Review
  12. Review
  13. Article
  14. Review
  15. Ubiquitin System-Driven Proteostasis in DNA Damage Response.International journal of molecular sciences · 2026
    Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Targeting ubiquitination in disease and therapy.Signal transduction and targeted therapy · 2025
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Yali XianDepartment of Dermatology & Venerology State Key Laboratory of Biotherapy West China Hospital Sichuan University Chengdu China.
Jing YeDepartment of Dermatology & Venerology State Key Laboratory of Biotherapy West China Hospital Sichuan University Chengdu China.
Yu TangDepartment of Dermatology & Venerology State Key Laboratory of Biotherapy West China Hospital Sichuan University Chengdu China.
Nan ZhangState Key Laboratory of Southwestern Chinese Medicine Resources School of Pharmacy Chengdu University of Traditional Chinese Medicine Chengdu China.
Cheng PengState Key Laboratory of Southwestern Chinese Medicine Resources School of Pharmacy Chengdu University of Traditional Chinese Medicine Chengdu China.
Wei HuangState Key Laboratory of Southwestern Chinese Medicine Resources School of Pharmacy Chengdu University of Traditional Chinese Medicine Chengdu China.
Gu HeDepartment of Dermatology & Venerology State Key Laboratory of Biotherapy West China Hospital Sichuan University Chengdu China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Deubiquitinating enzymes (DUBs) regulate substrate ubiquitination by removing ubiquitin or cleaving within ubiquitin chains, thereby maintaining cellular homeostasis. Approximately 100 DUBs in humans counteract E3 ubiquitin ligases, finely balancing ubiquitination and deubiquitination processes to maintain cellular proteostasis and respond to various stimuli and stresses. Given their role in modulating ubiquitination levels of various substrates, DUBs are increasingly linked to human health and disease. Here, we review the DUB family, highlighting their distinctive structural characteristics and chain-type specificities. We show that DUB family members regulate key signaling pathways, such as NF-κB, PI3K/Akt/mTOR, and MAPK, and play crucial roles in tumorigenesis and other diseases (neurodegenerative disorders, cardiovascular diseases, inflammatory disorders, and developmental diseases), making them promising therapeutic targets Our review also discusses the challenges in developing DUB inhibitors and underscores the critical role of the DUBs in cellular signaling and cancer. This comprehensive analysis enhances our understanding of the complex biological functions of the DUBs and underscores their therapeutic potential.

Indexed as

deubiquitinating enzymes (dubs)deubiquitinationhuman diseasessignaling pathway regulationtargeted therapy

Identifiers

PMID39678489
PMCPMC11645450

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.